Green N M, Toms E J
Biochem J. 1985 Oct 15;231(2):425-9. doi: 10.1042/bj2310425.
Cleavage of reduced, carboxymethylated, delipidated CA2+-transporting ATPase protein from rabbit sarcoplasmic reticulum with dimethyl sulphoxide/HBr yielded two long peptides (38 and 73 residues), distinct from the known major sequences of the ATPase. The longer peptide contained at least two cysteine residues, which were disulphide-linked in the native protein. It was therefore derived from the B-fragment of the ATPase in which the disulphides had previously been located. It probably formed a loop on the luminal side of the membrane, spanning two membrane-buried tryptophan residues. The N-terminal sequence of this peptide, (Trp)-Phe-Met-Tyr-Ala, forms the basis for an oligodeoxynucleotide probe, the use of which to identify cDNA corresponding to the ATPase is described elsewhere [MacLennan, Brandl, Korczak & Green (1985) Nature (London) 316, 696-700].
用二甲基亚砜/溴化氢切割来自兔肌浆网的还原型、羧甲基化、脱脂的钙离子转运ATP酶蛋白,产生了两条长肽(分别含38和73个残基),与ATP酶已知的主要序列不同。较长的肽含有至少两个半胱氨酸残基,它们在天然蛋白中形成二硫键连接。因此它源自ATP酶的B片段,之前二硫键就位于该片段中。它可能在膜的腔面形成一个环,跨越两个埋在膜内的色氨酸残基。该肽的N端序列(色氨酸)-苯丙氨酸-甲硫氨酸-酪氨酸-丙氨酸,构成了一个寡脱氧核苷酸探针的基础,关于用其鉴定与ATP酶对应的cDNA的方法已在其他地方描述 [麦克伦南、布兰德l、科尔扎克和格林(1985年)《自然》(伦敦)316, 696 - 700]。